Abstract:
:Arsenic, a curative agent for acute promyelocytic leukemia, induces cell apoptosis and degradation of BCR-ABL in chronic myelogenous leukemia (CML). We demonstrated that ubiquitination and degradation of BCR-ABL was mediated by c-CBL, a RING-type E3 ligase that was also shown to be involved in ubiquitination for many other receptor/protein tyrosine kinases. Our data showed that c-CBL protein was considerably up-regulated by arsenic sulfide (As(4)S(4)). Interestingly, arsenic directly bound the RING finger domain of c-CBL to inhibit its self-ubiquitination/degradation without interfering with the enhancement of ubiquitination and subsequent proteolysis of its substrate BCR-ABL. Degradation of BCR-ABL due to c-CBL induction as a result of arsenic treatment was also observed in vivo in CML mice. These findings provide insight into the molecular mechanisms of arsenic and further support its therapeutic applications in CML in combination with tyrosine kinase inhibitors and potentially also in other malignancies involving aberrant receptor/protein tyrosine kinase signaling.
journal_name
Proc Natl Acad Sci U S Aauthors
Mao JH,Sun XY,Liu JX,Zhang QY,Liu P,Huang QH,Li KK,Chen Q,Chen Z,Chen SJdoi
10.1073/pnas.1016311108subject
Has Abstractpub_date
2010-12-14 00:00:00pages
21683-8issue
50eissn
0027-8424issn
1091-6490pii
1016311108journal_volume
107pub_type
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